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Title: <span style="font-size:11.0pt;font-family: "Times New Roman";mso-fareast-font-family:"Times New Roman";mso-bidi-font-family: Mangal;mso-ansi-language:EN-GB;mso-fareast-language:EN-US;mso-bidi-language: HI" lang="EN-GB">Nanoactivator mediated modifications in thermostable amylase from<i style="mso-bidi-font-style:normal"> Bacillus licheniformis</i></span>
Authors: Khairnar, Rajendra S
Mahabole, Megha P
Pathak, Anupama P
Keywords: <i style="mso-bidi-font-style:normal"><span style="font-size:9.0pt;font-family:"Times New Roman";mso-fareast-font-family: "Times New Roman";mso-bidi-font-family:Mangal;letter-spacing:-.2pt;mso-ansi-language: EN-GB;mso-fareast-language:EN-US;mso-bidi-language:HI" lang="EN-GB">Bacillus</span></i>
Thermostable amylase
Issue Date: Dec-2012
Publisher: NISCAIR-CSIR, India
Abstract: Gram-positive rod-shaped thermophilic bacteria were isolated using samples collected from terrestrial natural thermal spring located at Unkeshwar <span style="mso-bidi-font-style:italic">(Longitude 78.22 degree East to 78.34 degree East, Latitude 19 degree 34' North to 19 degree 40' North)<i>, </i>District Nanded, Maharashtra State, India. The isolates were then cultivated using selective media and identified using culture-dependent techniques. One prominent isolate (UN1) exhibited high temperature stability and remarkable amylase production and was identified as <i style="mso-bidi-font-style:normal">Bacillus licheniformis</i>. Amylase production was carried out in starch media and the enzyme was partially purified and characterized for optimization of pH and temperature. Amylolytic activity of the enzyme was determined. Nanoactivator-mediated modifications were carried out to enhance amylolytic activity of the partially purified amylase. Three-fold increase in catalytic efficiency of amylase was obtained after modification. </span>
Description: 468-471
ISSN: 0975-0959 (Online); 0301-1208 (Print)
Appears in Collections:IJBB Vol.49(6) [December 2012]

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